| IED ID | IndEnz0002010924 |
| Enzyme Type ID | protease010924 |
| Protein Name |
Prolyl endopeptidase EC 3.4.21.26 Post-proline cleaving enzyme Proline-specific endopeptidase PE PSE |
| Gene Name | f1pep1 |
| Organism | Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Weeksellaceae Elizabethkingia Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) |
| Enzyme Sequence | MKYNKLSVAVAAFAFAAVSAQNSNVLKYPETKKVSHTDTYFGTQVSDPYRWLEDDRAEDTKAWVQQEVKFTQDYLAQIPFRDQLKKQLMDIWNYEKISAPFKKGKYTYFSKNDGLQAQSVLYRKDAAGKTEVFLDPNKFSEKGTTSLASVSFNKKGTLVAYSISEGGSDWNKIIILDAETKKQLDETLLDVKFSGISWLGDEGFFYSSYDKPKEGSVLSGMTDKHKVYFHKLGTKQSQDELIIGGDKFPRRYIGAYVTDDQRYLVVSAANATNGNELYIKDLKNKTDFIPIITGFDSNVNVADTDGDTLYLFTDKDAPNKRLVKTTIQNPKAETWKDVIAETSEPLEINTGGGYFFATYMKDAIDQVKQYDKNGKLVRAIKLPGSGNASGFGGEKTEKDLYYSFTNYITPPTIFKYNVTTGNSEVYQKPKVKFNPENYVSEQVFYTSSDGTKIPMMISYKKGLKKDGKNPTILYSYGGFNISLQPAFSVVNAIWMENGGIYAVPNIRGGGEYGKKWHDAGTKMQKKNVFNDFIAAGEYLQKNGYTSKEYMALSGRSNGGLLVGATMTMRPDLAKVAFPGVGVLDMLRYNKFTAGAGWAYDYGTAEDSKEMFEYLKSYSPVHNVKAGTCYPSTMVITSDHDDRVVPAHSFKFGSELQAKQSCKNPILIRIETNAGHGAGRSTEQVVAENADLLSFALYEMGIKSLK |
| Enzyme Length | 705 |
| Uniprot Accession Number | P27028 |
| Absorption | |
| Active Site | ACT_SITE 556; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:1840588"; ACT_SITE 675; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; |
| DNA Binding | |
| EC Number | 3.4.21.26 |
| Enzyme Function | FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Direct protein sequencing;Hydrolase;Periplasm;Protease;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,707 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |